Amyloid fibrils from proteins have garnered significant attention from researchers due to their outstanding functional properties. This study aims to investigate the effects of different sodium tripolyphosphate (STPP) concentrations (0.4 %, 4.0 %, and 8.0 %, w/v) on the formation and functional properties of ovalbumin (OVA) amyloid fibrils under heating conditions. Thioflavin T (ThT) assay revealed that the addition of STPP significantly accelerated the fibril formation potential. The fibril formation mechanism was explored through circular dichroism (CD), hydrophobic interaction, zeta potential, and Fourier transform infrared (FTIR) spectral analyses. Hydrophobic interactions and electrostatic repulsion were found to be the main driving forces for fibril formation of STPP-modified OVA (POVA). TEM results showed that STPP concentration was the key factor for regulating the morphology of OVA fibrils, with filamentous and worm-like fibrils for 0.4 % and 4.0 % POVA, respectively, while aggregated fibrils for 8.0 % POVA, due to the decrease of hydrophobic interaction and electrostatic repulsion. The 4.0 % POVA fibrils had the best emulsification capacity and foaming properties. The emulsion stabilized with 4.0 % POVA was the most stable. Overall, this study elucidated the potential formation mechanism of POVA fibrils, providing an environmentally friendly idea for preparation of OVA fibrils. Meanwhile, it had great potential as delivery systems for food constituents.